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PDBsum entry 4e9c
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Transferase/transferase inhibitor
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PDB id
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4e9c
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PDB id:
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| Name: |
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Transferase/transferase inhibitor
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Title:
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The structure of the polo-box domain (pbd) of polo-like kinase 1 (plk1) in complex with ldpplhspta phosphopeptide
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Structure:
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Serine/threonine-protein kinase plk1. Chain: a. Synonym: polo-like kinase 1, plk-1, serine/threonine-protein kinase 13, stpk13. Engineered: yes. Ldpplhspta phosphopeptide. Chain: b. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: plk1, plk. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: solid phase peptide synthesis
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Resolution:
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1.70Å
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R-factor:
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0.194
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R-free:
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0.232
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Authors:
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P.Sledz,M.Hyvonen,S.Lang,C.J.Stubbs,C.Abell
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Key ref:
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P.Śledź
et al.
(2012).
High-throughput interrogation of ligand binding mode using a fluorescence-based assay.
Angew Chem Int Ed Engl,
51,
7680-7683.
PubMed id:
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Date:
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21-Mar-12
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Release date:
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10-Oct-12
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PROCHECK
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Headers
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References
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P53350
(PLK1_HUMAN) -
Serine/threonine-protein kinase PLK1 from Homo sapiens
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Seq:
Struc:
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603 a.a.
223 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.2.7.11.21
- polo kinase.
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Reaction:
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1.
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L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
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2.
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
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L-seryl-[protein]
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+
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ATP
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=
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O-phospho-L-seryl-[protein]
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+
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ADP
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+
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H(+)
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L-threonyl-[protein]
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+
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ATP
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=
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O-phospho-L-threonyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Angew Chem Int Ed Engl
51:7680-7683
(2012)
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PubMed id:
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High-throughput interrogation of ligand binding mode using a fluorescence-based assay.
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P.Śledź,
S.Lang,
C.J.Stubbs,
C.Abell.
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ABSTRACT
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Probing the pocket: A high-throughput fluorescence-based thermal shift (FTS)
assay utilized different forms of a protein (in gray) to establish the binding
mode of a ligand (see picture). The assay serves in the rapid evaluation of
structure-activity binding-mode relationships for a series of ligands of Plk1,
an important target of anticancer therapy.
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Links
